http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CA-2435527-C

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_3e1018b924ad1e238642eaad9d2172a7
classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/D21C5-005
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/D21C9-1036
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classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/D21C5-00
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-24
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filingDate 2002-11-20-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2014-01-21-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_977ece4b1dd4bc6d9ad52cfac6be436e
publicationDate 2014-01-21-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CA-2435527-C
titleOfInvention Xylanases with enhanced thermophilicity and alkalophilicity
abstract The present invention provides a xylanase, or a modified xylanase enzyme comprising at least one substituted amino acid residue at a position selected from the group consisting of amino acid 11, 116, 118, 144 and 161, the position determined from sequence alignment of the modified xylanase with Trichoderma reesei xylanase II amino acid sequence. The xylanases described herein exhibit improved thermophilicity, alkalophilicity, expression efficiency, or a combination thereof, in comparison to a corresponding native xylanase.
priorityDate 2001-11-21-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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Total number of triples: 793.